3HNZ
Structure of E. coli FabF(C163A) in Complex with Platensimycin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004315 | molecular_function | 3-oxoacyl-[acyl-carrier-protein] synthase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006631 | biological_process | fatty acid metabolic process |
| A | 0006633 | biological_process | fatty acid biosynthetic process |
| A | 0009409 | biological_process | response to cold |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| A | 0019367 | biological_process | fatty acid elongation, saturated fatty acid |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 1903966 | biological_process | monounsaturated fatty acid biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE PMN A 413 |
| Chain | Residue |
| A | ALA163 |
| A | ALA309 |
| A | GLY310 |
| A | HIS340 |
| A | PHE398 |
| A | GLY399 |
| A | PHE400 |
| A | HOH431 |
| A | HOH464 |
| A | HOH472 |
| A | ALA205 |
| A | ARG206 |
| A | THR270 |
| A | SER271 |
| A | PRO272 |
| A | HIS303 |
| A | THR307 |
| A | PRO308 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 409 |
| Details | Domain: {"description":"Ketosynthase family 3 (KS3)","evidences":[{"source":"PROSITE-ProRule","id":"PRU01348","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"For beta-ketoacyl synthase activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU01348","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10037680","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9482715","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"For beta-ketoacyl synthase activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU01348","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16710421","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19233644","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19581087","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2GFX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3G0Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3G11","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3HNZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3I8P","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16710421","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19233644","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2GFX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3G0Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3G11","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 574 |
| Chain | Residue | Details |
| A | ALA163 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | HIS303 | activator, proton acceptor, proton donor |
| A | GLU314 | electrostatic stabiliser |
| A | LYS335 | electrostatic stabiliser |
| A | HIS340 | electrostatic stabiliser, hydrogen bond donor |
| A | PHE400 | electrostatic stabiliser |
